Probing the Role of Sigma π Interaction and Energetics in the Catalytic Efficiency of Endo-1,4-β-Xylanase
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Formidling
Chaetomium globosum endo-1,4-β-xylanase (XylCg) is distinguished from other xylanases by its high turnover rate (1,860 s−1), the highest ever reported for fungal xylanases. One conserved amino acid, W48, in the substrate binding pocket of wild-type XylCg was identified as an important residue affecting XylCg's catalytic efficiency.
Originalsprog | Engelsk |
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Tidsskrift | Applied and Environmental Microbiology |
Vol/bind | 78 |
Udgave nummer | 24 |
Sider (fra-til) | 8817-8821 |
Antal sider | 5 |
ISSN | 0099-2240 |
DOI | |
Status | Udgivet - 2012 |
ID: 229903076